HIP peptide

HIP peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-GQVELGGGNAVEVLK-OH

H-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Asn-Ala-Val-Glu-Val-Leu-Lys-OH

15

95.48%

C₆₃H₁₀₈N₁₈O₂₂

1469.63

Synthetic

Powder

HIP (hybrid insulin peptide) is a peptide derived from the splicing of insulin and islet amyloid polypeptides. It generates a preferred peptide-binding motif for HLA-DQ8, a genetic risk factor in type I diabetes. HIP is recognized by autoreactive CD4+ T cells, which are involved in the development of type I diabetes. Understanding the mechanism of recognition of HIP peptides by T cells can help in the development of therapies for type I diabetes. The crystal structure of TRBV5+ TCR-HLA-DQ8-HIP complexes provides insights into the recognition mechanism of HIP peptides by T cells, which can be useful in designing peptide-based therapies for type I diabetes.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Tran MT, Faridi P, Lim JJ, Ting YT, Onwukwe G, Bhattacharjee P, Jones CM, Tresoldi E, Cameron FJ, La Gruta NL, Purcell AW, Mannering SI, Rossjohn J, Reid HH. T cell receptor recognition of hybrid insulin peptides bound to HLA-DQ8. Nat Commun. 2021 Aug 25;12(1):5110. doi: 10.1038/s41467-021-25404-x. PMID: 34433824; PMCID: PMC8387461.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.